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- Currently displaying 1 - 20 of 987 publications
Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates
(2024)
(doi: 10.1101/2024.04.16.589709)
Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning
– Nature Chemical Biology
(2024)
(doi: 10.1038/s41589-024-01580-x)
RASP: Optimal Single Puncta Detection in Complex Cellular Backgrounds.
– The Journal of Physical Chemistry B
(2024)
128,
3585
(doi: 10.1021/acs.jpcb.4c00174)
Selenium-silk microgels as antifungal and antibacterial agents †
– Nanoscale horizons
(2024)
9,
609
(doi: 10.1039/d3nh00385j)
Single-Molecule Characterization and Super-Resolution Imaging of Alzheimer’s Disease-Relevant Tau Aggregates in Human Samples
– Angewandte Chemie International Edition
(2024)
e202317756
(doi: 10.1002/ange.202317756)
Single-Molecule Characterization and Super-Resolution Imaging of Alzheimer's Disease-Relevant Tau Aggregates in Human Samples.
– Angewandte Chemie International Edition
(2024)
e202317756
(doi: 10.1002/anie.202317756)
Design of amyloidogenic peptide traps
– Nature Chemical Biology
(2024)
1
(doi: 10.1038/s41589-024-01578-5)
High-density volumetric super-resolution microscopy.
– Nat Commun
(2024)
15,
1940
(doi: 10.1038/s41467-024-45828-5)
High-density volumetric super-resolution microscopy
– Nature Communications
(2024)
15,
1940
(doi: 10.1038/s41467-024-45828-5)
A Relationship between the Structures and Neurotoxic Effects of Aβ Oligomers Stabilized by Different Metal Ions.
– ACS Chemical Neuroscience
(2024)
15,
1125
(doi: 10.1021/acschemneuro.3c00718)
Large-scale visualisation of α-synuclein oligomers in Parkinson's disease brain tissue
(2024)
(doi: 10.1101/2024.02.17.580698)
Antibody agonists trigger immune receptor signaling through local exclusion of receptor-type protein tyrosine phosphatases.
– Immunity
(2024)
57,
256
(doi: 10.1016/j.immuni.2024.01.007)
Cathepsin B Processing Is Required for the In Vivo Efficacy of Albumin–Drug Conjugates
– Bioconjugate Chemistry
(2024)
35,
132
Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites.
– Proc Natl Acad Sci U S A
(2024)
121,
e2220075121
(doi: 10.1073/pnas.2220075121)
Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils.
– Communications biology
(2024)
7,
153
(doi: 10.1038/s42003-024-05858-7)
Temperature-induced changes in protein interactions control RNA recruitment to G3BP1 condensates
(2024)
(doi: 10.1101/2024.02.02.578543)
Thermodynamics of temperature modulation in biomolecular phase separation
– Biophysical Journal
(2024)
123,
495a
(doi: 10.1016/j.bpj.2023.11.2994)
Molecular chaperones and their role in amyloid formation
– Biophysical Journal
(2024)
123,
301a
(doi: 10.1016/j.bpj.2023.11.1869)
Novel methods to study amyloid oligomers
– Biophysical Journal
(2024)
123,
41a
(doi: 10.1016/j.bpj.2023.11.331)
The Alzheimer’s Aβ peptide forms biomolecular condensates that trigger amyloid aggregation
(2024)
(doi: 10.1101/2024.01.14.575549)